(data stored in SCRATCH zone)

SWISSPROT: Q8KYB3_LISMN

ID   Q8KYB3_LISMN            Unreviewed;       504 AA.
AC   Q8KYB3;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   11-DEC-2019, entry version 63.
DE   RecName: Full=Cardiolipin synthase {ECO:0000256|HAMAP-Rule:MF_01916};
DE            Short=CL synthase {ECO:0000256|HAMAP-Rule:MF_01916};
DE            EC=2.7.8.- {ECO:0000256|HAMAP-Rule:MF_01916};
GN   Name=cls {ECO:0000313|EMBL:AAM48484.1};
OS   Listeria monocytogenes.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1639 {ECO:0000313|EMBL:AAM48484.1};
RN   [1] {ECO:0000313|EMBL:AAM48484.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=EGD {ECO:0000313|EMBL:AAM48484.1};
RX   PubMed=12039883; DOI=10.1093/jac/dkf065;
RA   Lampidis R., Kostrewa D., Hof H.;
RT   "Molecular characterization of the genes encoding DNA gyrase and
RT   topoisomerase IV of Listeria monocytogenes.";
RL   J. Antimicrob. Chemother. 49:917-924(2002).
CC   -!- FUNCTION: Catalyzes the reversible phosphatidyl group transfer from one
CC       phosphatidylglycerol molecule to another to form cardiolipin (CL)
CC       (diphosphatidylglycerol) and glycerol. {ECO:0000256|HAMAP-
CC       Rule:MF_01916, ECO:0000256|SAAS:SAAS00006089}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a
CC         cardiolipin + glycerol; Xref=Rhea:RHEA:31451, ChEBI:CHEBI:17754,
CC         ChEBI:CHEBI:62237, ChEBI:CHEBI:64716; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01916, ECO:0000256|SAAS:SAAS01117805};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01916};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01916}.
CC   -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01916,
CC       ECO:0000256|SAAS:SAAS00538679}.
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DR   EMBL; AF084042; AAM48484.1; -; Genomic_DNA.
DR   eggNOG; ENOG4105CQX; Bacteria.
DR   eggNOG; COG1502; LUCA.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008808; F:cardiolipin synthase activity; IEA:InterPro.
DR   GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_01916; Cardiolipin_synth_Cls; 1.
DR   InterPro; IPR030874; Cardiolipin_synth_Firmi.
DR   InterPro; IPR022924; Cardiolipin_synthase.
DR   InterPro; IPR027379; CLS_N.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   Pfam; PF13091; PLDc_2; 2.
DR   Pfam; PF13396; PLDc_N; 1.
DR   SMART; SM00155; PLDc; 2.
DR   TIGRFAMs; TIGR04265; bac_cardiolipin; 1.
DR   PROSITE; PS50035; PLD; 2.
PE   3: Inferred from homology;
DR   PRODOM; Q8KYB3.
DR   SWISS-2DPAGE; Q8KYB3.
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01916,
KW   ECO:0000256|SAAS:SAAS00117509};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01916,
KW   ECO:0000256|SAAS:SAAS00006181};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01916,
KW   ECO:0000256|SAAS:SAAS00301903};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01916, ECO:0000256|SAAS:SAAS00016851};
KW   Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01916,
KW   ECO:0000256|SAAS:SAAS00301877};
KW   Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_01916,
KW   ECO:0000256|SAAS:SAAS00006188}; Repeat {ECO:0000256|SAAS:SAAS00723978};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01916,
KW   ECO:0000256|SAAS:SAAS00420582};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01916,
KW   ECO:0000256|SAAS:SAAS00420576};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01916,
KW   ECO:0000256|SAAS:SAAS00016984}.
FT   TRANSMEM        5..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   TRANSMEM        28..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   TRANSMEM        61..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   DOMAIN          231..258
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          416..443
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   ACT_SITE        236
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   ACT_SITE        238
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   ACT_SITE        243
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   ACT_SITE        421
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   ACT_SITE        423
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   ACT_SITE        428
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ   SEQUENCE   504 AA;  56697 MW;  80281D86156BE604 CRC64;
     MRKLIQFLFI AVVLFLVEYV LINQAAILFL VTSGIIQLCG VIIAIRLLLF DQRNTSSKVA
     WVAVIFILPV LGTISYLVFG RNPATRKFST AQVKEKTKLI NAIHAIPNNT NEKLPRLSKR
     IAHLTSIEPI KGNKIEILTN GEETFPVLLD ALRKAENHIH IQYYIFKTDA ISTEIRDILV
     EKAKSGVEVR FMFDGLGSSK LGKAFLAPLK EAGVSIHAFD PIASPWIVRT ANLRNHRKIV
     VIDGQIGFTG GLNIGEEYRS NTPDFRVWRD THIKITGQAV IELQESFLND WVYMENQAGA
     ADGFISESGS KQYFSPVDMG DEWAQVIYGG PYDKEKWVRD SMLDLIDSAK ESVWIVSPYF
     VPDEESLAVI RRVAMSGVDV RVIIPGKGDR GTSFHGSNAY VKTMIEAGAK MYAYADDSFV
     HAKAMLVDGT RAAIGTANFD VRSFRLNHEL MVFLYDESEA MHHLKRDFKK DFEDSRLFTM
     KDMENKPLLT RIKEVLSSLL SPIL
//

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